Functional Information from GO Data
Chain | GOid | namespace | contents |
E | 0004222 | molecular_function | metalloendopeptidase activity |
E | 0006508 | biological_process | proteolysis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | binding site for residue 5H8 E 401 |
Chain | Residue |
E | TYR106 |
E | TYR157 |
E | GLU166 |
E | LEU202 |
E | ARG203 |
E | HIS231 |
E | ZN402 |
E | DMS409 |
E | DMS409 |
E | GOL411 |
E | HOH572 |
E | ASN111 |
E | HOH629 |
E | HOH679 |
E | ASN112 |
E | ALA113 |
E | PHE114 |
E | TRP115 |
E | HIS142 |
E | GLU143 |
E | HIS146 |
site_id | AC2 |
Number of Residues | 4 |
Details | binding site for residue ZN E 402 |
Chain | Residue |
E | HIS142 |
E | HIS146 |
E | GLU166 |
E | 5H8401 |
site_id | AC3 |
Number of Residues | 6 |
Details | binding site for residue CA E 403 |
Chain | Residue |
E | ASP138 |
E | GLU177 |
E | ASP185 |
E | GLU187 |
E | GLU190 |
E | HOH602 |
site_id | AC4 |
Number of Residues | 6 |
Details | binding site for residue CA E 404 |
Chain | Residue |
E | ASP57 |
E | ASP59 |
E | GLN61 |
E | HOH556 |
E | HOH605 |
E | HOH780 |
site_id | AC5 |
Number of Residues | 6 |
Details | binding site for residue CA E 405 |
Chain | Residue |
E | GLU177 |
E | ASN183 |
E | ASP185 |
E | GLU190 |
E | HOH560 |
E | HOH631 |
site_id | AC6 |
Number of Residues | 6 |
Details | binding site for residue CA E 406 |
Chain | Residue |
E | TYR193 |
E | THR194 |
E | ILE197 |
E | ASP200 |
E | HOH615 |
E | HOH751 |
site_id | AC7 |
Number of Residues | 5 |
Details | binding site for residue DMS E 407 |
Chain | Residue |
E | ILE1 |
E | THR2 |
E | GLY3 |
E | GLN31 |
E | ASN33 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue DMS E 408 |
Chain | Residue |
E | GLY95 |
E | PRO184 |
E | TRP186 |
E | HOH666 |
E | HOH688 |
site_id | AC9 |
Number of Residues | 5 |
Details | binding site for residue DMS E 409 |
Chain | Residue |
E | TYR110 |
E | ASN112 |
E | PHE114 |
E | 5H8401 |
E | 5H8401 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue DMS E 410 |
Chain | Residue |
E | TYR66 |
E | HIS216 |
E | SER218 |
E | TYR251 |
E | HOH867 |
E | HOH873 |
site_id | AD2 |
Number of Residues | 8 |
Details | binding site for residue GOL E 411 |
Chain | Residue |
E | PHE114 |
E | TRP115 |
E | HIS146 |
E | TYR157 |
E | 5H8401 |
E | HOH513 |
E | HOH536 |
E | HOH703 |
site_id | AD3 |
Number of Residues | 7 |
Details | binding site for residue GOL E 412 |
Chain | Residue |
E | GLY109 |
E | TYR110 |
E | ASN111 |
E | ASN112 |
E | GLN158 |
E | HOH616 |
E | HOH756 |
site_id | AD4 |
Number of Residues | 12 |
Details | binding site for residue GOL E 413 |
Chain | Residue |
E | GLY247 |
E | GLY248 |
E | THR249 |
E | VAL255 |
E | GLN273 |
E | TYR274 |
E | LEU275 |
E | HOH553 |
E | HOH558 |
E | HOH654 |
E | HOH667 |
E | HOH766 |
Functional Information from PROSITE/UniProt
site_id | PS00142 |
Number of Residues | 10 |
Details | ZINC_PROTEASE Neutral zinc metallopeptidases, zinc-binding region signature. VVAHELTHAV |
Chain | Residue | Details |
E | VAL139-VAL148 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
E | GLU143 | |
Chain | Residue | Details |
E | HIS231 | |
site_id | SWS_FT_FI3 |
Number of Residues | 16 |
Details | BINDING: |
Chain | Residue | Details |
E | ASP57 | |
E | ASP185 | |
E | GLU187 | |
E | GLU190 | |
E | TYR193 | |
E | THR194 | |
E | ILE197 | |
E | ASP200 | |
E | ASP59 | |
E | GLN61 | |
E | ASP138 | |
E | HIS142 | |
E | HIS146 | |
E | GLU166 | |
E | GLU177 | |
E | ASN183 | |
Catalytic Information from CSA
site_id | MCSA1 |
Number of Residues | 7 |
Details | M-CSA 176 |
Chain | Residue | Details |
E | HIS142 | metal ligand |
E | GLU143 | electrostatic stabiliser, metal ligand |
E | HIS146 | metal ligand |
E | TYR157 | electrostatic stabiliser, hydrogen bond donor, steric role |
E | GLU166 | metal ligand |
E | ASP226 | activator, electrostatic stabiliser, hydrogen bond acceptor |
E | HIS231 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |